1HF9

C-Terminal Coiled-Coil Domain from Bovine IF1

Summary for 1HF9

• Entry DOI: 10.2210/pdb1hf9/pdb
• NMR Information: BMRB: 4906
• Descriptor: ATPASE INHIBITOR (MITOCHONDRIAL) (1 entity in total)
• Functional Keywords: atpase inhibitor, f1 atpase inhibitor, mitochondrion, transit peptide
• Biological source: BOS TAURUS (COW)
• Total number of polymer chains: 2
• Total formula weight: 9999.23

Authors

Gordon-Smith, D.J.,Carbajo, R.J.,Yang, J.-C.,Videler, H.,Runswick, M.J.,Walker, J.E.,Neuhaus, D. (deposition date: 2000-11-30, release date: 2001-05-31, Last modification date: 2024-05-15)

Primary citation

Gordon-Smith, D.J.,Carbajo, R.J.,Yang, J.C.,Videler, H.,Runswick, M.J.,Walker, J.E.,Neuhaus, D.
Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.
J. Mol. Biol., 308:325-339, 2001

PubMed Abstract: Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface.

PubMed: 11327770
DOI: 10.1006/jmbi.2001.4570

Experimental method

SOLUTION NMR